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関連する概念動画

The Sarcomere01:08

The Sarcomere

8.2K
A sarcomere is a microscopic segment repeating in a myofibril. The sarcomere fundamentally consists of two main myofilaments: thick filaments called myosin and thin filaments called actin. These filaments interact by sliding past each other in response to stimulus. In addition to myosin and actin, several other proteins, such as tropomyosin, troponin, titin, nebulin, myomesin, α-actinin, and dystrophin, play crucial roles in regulating, structuring, and functioning of the sarcomere.
Each...
8.2K
Actin and Myosin in Muscle Contraction01:16

Actin and Myosin in Muscle Contraction

11.9K
Actin and myosin are contractile proteins that form the sarcomere found in skeletal muscle tissues for regulating muscle contraction. Actin, a globular contractile protein, interacts with myosin for muscle contraction. The skeletal tissue appears striped or striated under a microscope due to the repeated arrangement of contractile proteins actin and myosin along the length of myofibrils. Dark A bands and light I bands repeat along myofibrils, and the alignment of myofibrils in the cell causes...
11.9K
Overview of Myosin Structure and Function01:15

Overview of Myosin Structure and Function

4.4K
Myosins are a family of molecular motor proteins, first identified in the skeletal muscles, where they are responsible for muscle contraction. Along with their role in muscle contraction, these proteins also play a role in the intracellular transport of molecules and vesicles. There are twenty-four classes of myosins based on their domain sequence and organization. Of the twenty-four, six classes (Myosin I, Myosin II, Myosin V, Myosin VI, Myosin VII, and Myosin X)  have been well...
4.4K
Structure of Cardiac Muscles01:13

Structure of Cardiac Muscles

11.9K
Cardiac muscle, or myocardium, is a specialized type of muscle found exclusively in the heart. Its unique structural and functional characteristics enable the heart to perform its vital role of pumping blood throughout the body continuously and rhythmically. The cardiac muscle cells, or cardiomyocytes, possess an endomysium and perimysium but do not have an epimysium.
Compared to skeletal muscles, cardiac muscle cells are small and mostly have a single nucleus. Additionally, they are usually...
11.9K
Overview of Skeletal Muscle01:15

Overview of Skeletal Muscle

11.8K
Skeletal muscles are composed of a bundle of muscle fibers and are attached to bones through tendons. Each skeletal muscle fiber is a single muscle cell. The sarcolemma, the plasma membrane of a skeletal muscle cell, consists of a lipid bilayer and glycocalyx that supports muscle fibers. The sarcolemma extends into the muscle cells to form tubular structures called transverse or T-tubules. Each side of the T-tubules consists of a membrane-bound structure called the sarcoplasmic reticulum,...
11.8K
Relaxation of Skeletal Muscles01:29

Relaxation of Skeletal Muscles

3.3K
The period of muscle contraction primarily influences the duration of stimulation at the neuromuscular junction (NMJ), the presence of free calcium ions in the sarcoplasm, and the availability of energy or ATP to support contractions.
When an action potential reaches the axon terminal, it depolarizes the membrane and opens voltage-gated sodium channels. Sodium ions enter the cell, further depolarizing the presynaptic membrane. This depolarization causes voltage-gated calcium channels to open....
3.3K

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関連する実験動画

Updated: Jul 12, 2025

Isolating Myofibrils from Skeletal Muscle Biopsies and Determining Contractile Function with a Nano-Newton Resolution Force Transducer
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Isolating Myofibrils from Skeletal Muscle Biopsies and Determining Contractile Function with a Nano-Newton Resolution Force Transducer

Published on: May 7, 2020

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リラックスした心臓のサルコメアのネイティブミオシンフィラメントの構造

Davide Tamborrini1, Zhexin Wang1,2, Thorsten Wagner1

  • 1Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany.

Nature
|November 2, 2023
PubMed
まとめ

この研究では,冷凍電子トモグラフィを用いた心臓サルコメアの厚い繊維の3D分子構造を明らかにした. ミオシン,チチン,ミオシン結合タンパク質 C (MyBP-C) の組織を詳細に説明し,筋肉の機能と病気の洞察を提供します.

さらに関連する動画

Assessment of Myofilament Ca2+ Sensitivity Underlying Cardiac Excitation-contraction Coupling
08:29

Assessment of Myofilament Ca2+ Sensitivity Underlying Cardiac Excitation-contraction Coupling

Published on: August 1, 2016

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Simultaneous Brightfield, Fluorescence, and Optical Coherence Tomographic Imaging of Contracting Cardiac Trabeculae Ex Vivo
12:54

Simultaneous Brightfield, Fluorescence, and Optical Coherence Tomographic Imaging of Contracting Cardiac Trabeculae Ex Vivo

Published on: October 2, 2021

3.3K

関連する実験動画

Last Updated: Jul 12, 2025

Isolating Myofibrils from Skeletal Muscle Biopsies and Determining Contractile Function with a Nano-Newton Resolution Force Transducer
07:55

Isolating Myofibrils from Skeletal Muscle Biopsies and Determining Contractile Function with a Nano-Newton Resolution Force Transducer

Published on: May 7, 2020

7.1K
Assessment of Myofilament Ca2+ Sensitivity Underlying Cardiac Excitation-contraction Coupling
08:29

Assessment of Myofilament Ca2+ Sensitivity Underlying Cardiac Excitation-contraction Coupling

Published on: August 1, 2016

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Simultaneous Brightfield, Fluorescence, and Optical Coherence Tomographic Imaging of Contracting Cardiac Trabeculae Ex Vivo
12:54

Simultaneous Brightfield, Fluorescence, and Optical Coherence Tomographic Imaging of Contracting Cardiac Trabeculae Ex Vivo

Published on: October 2, 2021

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科学分野:

  • 構造生物学
  • 筋肉生理学

背景:

  • 厚い繊維はサルコメアの重要な成分であり,そのタンパク質の変異は心臓と筋肉の病気と関連しています.
  • 厚い繊維の正確な分子組織は ほとんど不明です

研究 の 目的:

  • リラックス状態の原始的な心臓サルコメアの分子構造を決定する.
  • 厚いフィラメント内のミオシン,チチン,およびミオシン結合タンパク質C (MyBP-C) の3次元の配置を解明する.

主な方法:

  • 冷凍電子トモグラフィーは,本来の心臓のサルコメアを再現するために使用されました.
  • 基礎分子組織を理解するために リラックス状態に焦点を当てました

主要な成果:

  • 厚いフィラメントの詳細な3D再構築は,ミオシン配列の位置的変化を明らかにし,特殊な機能を示唆しました.
  • 3組のチチン-αとチチン-β鎖が軸に沿って運行し,ミオシンの尾と相互作用し,潜在的にサルコメアの活性化を調節することが判明した.
  • ミオシン結合タンパク質C (MyBP-C) は,薄いフィラメントと厚いフィラメントを橋渡しし,ミオシンヘッドを予期せぬ方法で安定させることが観察されました.

結論:

  • この研究は心臓の厚いフィラメントの 分子詳細を 提供しています
  • 発見は,サルコメリックタンパク質に関連する筋肉疾患を理解するための構造的基礎を提供します.
  • ミオシンヘッドの安定化における MyBP-C の発見は,研究のための新しい道を開きます.